| DOI | Resolve DOI: https://doi.org/10.1021/bi000224u |
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| Author | Search for: Bradshaw, Jeremy P.; Search for: Darkes, Malcolm J. M.; Search for: Harroun, Thad A.; Search for: Katsaras, John1; Search for: Epand, Richard M. |
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| Affiliation | - National Research Council of Canada. NRC Steacie Institute for Molecular Sciences
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| Format | Text, Article |
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| Abstract | Fusion peptides mimic the membrane fusion activities of the larger viral proteins from which they derive their sequences. A possible mode of activity involves their oblique insertion into lipid bilayers, causing membrane disruption by promoting highly curved hemifusion intermediates, leading to fusion. We have determined the location and orientation of the simian immunodeficiency virus (SIV) fusion peptide in planar lipid bilayers using neutron lamellar diffraction. The helical axis of the peptide adopts an angle of 55 relative to the membrane normal, while it positions itself nearest the lipid bilayer surface. This is the first direct observation of the structural interaction between a fusion peptide and a phospholipid bilayer. |
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| Publication date | 2000-05-11 |
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| In | |
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| Language | English |
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| NPARC number | 12328508 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | bdfe3643-de7a-4c61-93c2-0dbb46ed03cc |
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| Record created | 2009-09-10 |
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| Record modified | 2020-03-26 |
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